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1TJD

The crystal structure of the reduced disulphide bond isomerase, DsbC, from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003756molecular_functionprotein disulfide isomerase activity
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042803molecular_functionprotein homodimerization activity
A0046688biological_processresponse to copper ion
A0061077biological_processchaperone-mediated protein folding
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. ITvFTdiTCGYCHkLheqM
ChainResidueDetails
AILE90-MET108

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eej
ChainResidueDetails
ACYS98
ATYR100
ACYS101
AARG125

site_idMCSA1
Number of Residues4
DetailsM-CSA 512
ChainResidueDetails
AASP95increase nucleophilicity, proton acceptor, proton donor
ACYS98electrofuge, electrophile, nucleofuge, nucleophile, proton acceptor, proton donor
ACYS101nucleophile, proton donor
AARG125increase nucleophilicity

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PDB entries from 2024-07-10

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